Varicella-zoster virus gH:gL contains a structure reactive with the anti-human gamma chain of IgG near the glycosylation site
Department of Virology, Toyama Medical and Pharmaceutical University, 2630 Sugitani, Toyama 930-01, Japan 1 Teijin Institute for Biomedical Research, Asahigaoka 4-3-2, Hino, Tokyo 191, Japan 2 Author for correspondence: Kimiyasu Shiraki. Fax +81 76 434 5020. e-mail kshiraki{at}toyama-mpu.ac.jp Varic...
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Published in | Journal of general virology Vol. 82; no. 2; pp. 331 - 334 |
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Main Authors | , , , , , , , , |
Format | Journal Article |
Language | English |
Published |
England
Soc General Microbiol
01.02.2001
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Subjects | |
Online Access | Get full text |
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Summary: | Department of Virology, Toyama Medical and Pharmaceutical University, 2630 Sugitani, Toyama 930-01, Japan 1
Teijin Institute for Biomedical Research, Asahigaoka 4-3-2, Hino, Tokyo 191, Japan 2
Author for correspondence: Kimiyasu Shiraki. Fax +81 76 434 5020. e-mail kshiraki{at}toyama-mpu.ac.jp
Varicella-zoster virus (VZV) glycoproteins were purified from infected cells using monoclonal antibodies and gH:gL was found to react with antibodies to the chain of human IgG (h-IgG), whereas gE:gI and gB did not. When gH:gL was captured by concanavalin A, it lost reactivity with the anti-h-IgG chain (anti-h- -IgG). gH:gL reacted with anti-h- -IgG in an ELISA assay and gave a K d value of 2·16 x 10 -7 M in a BIAcore assay. The K d value of the human monoclonal antibody to gH (TI-57) used for the purification of gH:gL was 4·45 x 10 -10 M. Virus pretreated with anti-h-IgG was five times more resistant to neutralization with TI-57. Although the nature of the binding was not clear, gH:gL bound to anti-h- -IgG. If this interaction results from immunological similarity between gH:gL and h-IgG, it may cause immune evasion in the pathogenesis of VZV infection. |
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Bibliography: | ObjectType-Article-2 SourceType-Scholarly Journals-1 ObjectType-Feature-1 content type line 23 ObjectType-Article-1 ObjectType-Feature-2 |
ISSN: | 0022-1317 1465-2099 |
DOI: | 10.1099/0022-1317-82-2-331 |